|
Name |
Accession |
Description |
Interval |
E-value |
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
41-596 |
0e+00 |
|
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection.
Pssm-ID: 188652 [Multi-domain] Cd Length: 558 Bit Score: 936.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 41 YDGWYNNLANSEWGSAGSRLHRDARSYYSDGVYSVNNS-LPSARELSDILFKGESGIPNTRGCTTLLAFFSQVVAYEIMQ 119
Cdd:cd09820 1 YDGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEeRPNPRSLSNLLMKGESGLPSTRNRTALLVFFGQHVVSEILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 120 SNGVSCPLETLKIQVPLCDNVFDNECEGKTTIPFYRAKYDKATGNGLNSPREQINERTSWIDGSFIYGTTQPWVSALRSF 199
Cdd:cd09820 81 ASRPGCPPEYFNIEIPKGDPVFDPECTGNIELPFQRSRYDKNTGYSPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 200 KQGRLAEGV-PGYPPLNNPHIPLNNPAPPQVHRLMSPDRLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIYREHPDWT 278
Cdd:cd09820 161 SGGRLASGDdGGFPRRNTNRLPLANPPPPSYHGTRGPERLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 279 DEQIFQAARRLVIASMQKIIAYDFVPGLLGEDVrlSNYTKYMPHVPPGISHAFGAAAFRFPHSIVPPAMLLRKRGNK-CE 357
Cdd:cd09820 241 DEDIFQEARKWVIATYQNIVFYEWLPALLGTNV--PPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVYRRNRQCNfRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 358 FRTEVGGYPALRLCQNWWNAQDIVKEYSVDEIILGMASQIAERDDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGV 437
Cdd:cd09820 319 VLTTSGGSPALRLCNTYWNSQEPLLKSDIDELLLGMASQIAEREDNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDHGL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 438 PPYNELRRTFGLAP-KTWETMNEDFYKKHTAKVEKLKELYGGNILYLDAYVGGMLEGGENGPGEMFKEIIKDQFTRIRDG 516
Cdd:cd09820 399 PDYNTAREAFGLPPrTTWSDINPDLFKKDPELLERLAELYGNDLSKLDLYVGGMLESKGGGPGELFRAIILDQFQRLRDG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 517 DRFWFENKLNRLFTDEEVQMIHSITLRDIIKATTDIDETMLQKDVFFFKEGDPCPQPFQVNTIGLEPCAPLIQSTYWDDN 596
Cdd:cd09820 479 DRFWFENVKNGLFTAEEIEEIRNTTLRDVILAVTDIDNTDLQKNVFFWKNGDPCPQPKQLTENMLEPCTPLTVYDYFEGS 558
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
39-562 |
1.82e-176 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 537.91 E-value: 1.82e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 39 QRYDGWYNNLANSEWGSAGSRLHRDARSYYSDGVY-----SVNNSLPSARELSDILFKGESGIPNTRgCTTLLAFFSQVV 113
Cdd:pfam03098 2 RTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSaprgsSSGSPLPSPRLVSNKLFAGDSGIPDPN-LTLLLMQWGQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 114 AYEIMQSNGVSCPLET---------------LKIQVPLCDNVFDNEceGKTTIPFYRAKYDKATGNglnsPREQINERTS 178
Cdd:pfam03098 81 DHDLTLTPESTSPNGSscdcccppenlhppcFPIPIPPDDPFFSPF--GVRCMPFVRSAPGCGLGN----PREQINQVTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 179 WIDGSFIYGTTQPWVSALRSFKQGRLAEGVP----GYPPLNNPHIPLNNPAPPQVhrlmspdrLFMLGDSRVNENPGLLS 254
Cdd:pfam03098 155 FLDGSQVYGSSEETARSLRSFSGGLLKVNRSddgkELLPFDPDGPCCCNSSGGVP--------CFLAGDSRANENPGLTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 255 FGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDV------RLSNYTKYMPHVPPGIS 328
Cdd:pfam03098 227 LHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNmnwfglLPLPYNGYDPNVDPSIS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 329 HAFGAAAFRFPHSIVPPAMLLRkrgNKCEFRTEvggyPALRLCQNWWNAQDIVkEYSVDEIILGMASQIAERDDNIVVED 408
Cdd:pfam03098 307 NEFATAAFRFGHSLIPPFLYRL---DENNVPEE----PSLRLHDSFFNPDRLY-EGGIDPLLRGLATQPAQAVDNNFTEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 409 LRDYIFGPM-HFSRLDVVASSIMRGRDNGVPPYNELRRTFGL-APKTWETMNEDFykkHTAKVEKLKELYgGNILYLDAY 486
Cdd:pfam03098 379 LTNHLFGPPgEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLpPAKSFEDLTDVI---PNEVIAKLRELY-GSVDDIDLW 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507545 487 VGGMLEGGENG--PGEMFKEIIKDQFTRIRDGDRFWFENKLNRLFTDEEVQMIHSITLRDIIKATTDIDETMlQKDVF 562
Cdd:pfam03098 455 VGGLAEKPLPGglVGPTFACIIGDQFRRLRDGDRFWYENGNQGSFTPEQLEEIRKTSLARVICDNTDIIETI-QPNVF 531
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
1224-1408 |
1.89e-42 |
|
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.
Pssm-ID: 99783 [Multi-domain] Cd Length: 210 Bit Score: 154.77 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1224 IAHAEILP-SDIIYIEYRRPREFEYKSGQWITVSSPSISCTFnESHAFSIASSPQDEN--MKLYIKAV-GPWTwKLRSEL 1299
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLLSFW-QSHPFTIASSPEDEQdtLSLIIRAKkGFTT-RLLRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1300 IRSLNTGSPFPlIHMKGPYGDGNQEWMNYEVAIMVGAGIGVTPYASTLVDLVQKTSSdsfhRVRCRKVYFLWVCSSHKNF 1379
Cdd:cd06186 79 LKSPGGGVSLK-VLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSK----TSRTRRVKLVWVVRDREDL 153
|
170 180 190
....*....|....*....|....*....|..
gi 17507545 1380 EWFVDML---KNVENQAkpgilETHIFVTQMF 1408
Cdd:cd06186 154 EWFLDELraaQELEVDG-----EIEIYVTRVV 180
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
1328-1484 |
1.94e-20 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 89.32 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1328 YEVAIMVGAGIGVTPYASTLVDLVQKTSSDsfhrvRCRKVYFLWVCSSHKNFEWFVDMLKNVENQaKPGILETHIFVTQM 1407
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKKL-----KTKKIKFYWVVRDLSSLEWFKDVLNELEEL-KELNIEIHIYLTGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1408 fhkfdlrttmlYICEKHFRATNSGIS--MFTGLHAKN--------HFGRPNFKAFFQFIQSEHKEQSeIGVFSCGPVNLN 1477
Cdd:pfam08030 75 -----------YEAEDASDQSDSSIRseNFDSLMNEVigvdfvefHFGRPNWKEVLKDIAKQHPNGS-IGVFSCGPPSLV 142
|
....*..
gi 17507545 1478 ESIAEGC 1484
Cdd:pfam08030 143 DELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
1045-1406 |
3.61e-18 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 90.68 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1045 CMALILLTVcrniitlLRETVIAQY--IPFDSAIAFHKIVALFTLFWSTLH--------TIGHcvnfyHVGTQSDRglac 1114
Cdd:PLN02844 166 CLALLLLPV-------LRGLALFRLlgIQFEASVRYHVWLGTSMIFFATVHgastlfiwGISH-----HIQDEIWK---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1115 lFQETFfgsdvvptlSYWFYGTITGLTGIglvivmsIIYVFALPKFTRRAYHAFRLTHLLNIGFYALTILHGlpslfGSP 1194
Cdd:PLN02844 230 -WQKTG---------RIYLAGEIALVTGL-------VIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHA-----GDR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1195 KFgYYVVGPIVLFVIDRIIGLMQYYKSLDIAHAEILPSDIIYIEYRRPREFEYKSGQWITVSSPSIScTFnESHAFSIAS 1274
Cdd:PLN02844 288 HF-YMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSIS-RF-QWHPFSITS 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1275 SPQ--DENMKLYIKAVGPWTWKLRSELIRSLNTGSP----FPlIHMKGPYGDGNQEWMNYEVAIMVGAGIGVTPYASTLV 1348
Cdd:PLN02844 365 SSNidDHTMSVIIKCEGGWTNSLYNKIQAELDSETNqmncIP-VAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILK 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1349 DLVQKTSSdsfhRVRC-RKVYFLWVCSSHKNFEWFVDMLKNVENQAKPGI-LETHIFVTQ 1406
Cdd:PLN02844 444 EIASQSSS----RYRFpKRVQLIYVVKKSQDICLLNPISSLLLNQSSNQLnLKLKVFVTQ 499
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
153-546 |
1.27e-17 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 88.67 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 153 FYRAKYDKATGNGLNSprEQINERTSWIDGSFIYGTTQPWVSALRSFKQGRLAEGVPGYPPLNNPHIPLNnpappqvhrl 232
Cdd:PLN02283 189 FYKTKEVPTGSPDIKT--GSLNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKISEDGLLLHDEDGIPIS---------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 233 mspdrlfmlGDSRvNENPGLLSFGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVP-------- 304
Cdd:PLN02283 257 ---------GDVR-NSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVellktdtl 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 305 ---------GLLGEDVR-------------LSNYTKYMPH-VPPGISHAFgAAAFRFpHSIVPPAMLLRkrgnkcefrtE 361
Cdd:PLN02283 327 lagmranwyGLLGKKFKdtfghiggpilsgLVGLKKPNNHgVPYSLTEEF-TSVYRM-HSLLPDHLILR----------D 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 362 VGGYPALRLCQnwwnaqDIVKEYSVDEII----------LGMASQIAE------------------RDdnIVVEDlRDYI 413
Cdd:PLN02283 395 ITAAPGENKSP------PLIEEIPMPELIglkgekklskIGFEKLMVSmghqacgalelwnypswmRD--LVPQD-IDGE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 414 FGPMHfsrLDVVASSIMRGRDNGVPPYNELRRTFGLAP-KTWETMNEDfykkhTAKVEKLKELYGGNILYLDAYVGGMLE 492
Cdd:PLN02283 466 DRPDH---VDMAALEIYRDRERGVARYNEFRRNLLMIPiSKWEDLTDD-----EEAIEVLREVYGDDVEKLDLLVGLMAE 537
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 17507545 493 ggENGPGEMFKEIIKDQF----TRIRDGDRFWFENKLNRLFTDEEVQMIHSI-TLRDII 546
Cdd:PLN02283 538 --KKIKGFAISETAFFIFllmaSRRLEADRFFTSNFNEKTYTKKGLEWVNTTeSLKDVI 594
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
989-1405 |
3.14e-17 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 86.10 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 989 TYRQHVFIIFCFVAINIVLFFELFWHSRYLNEDRDLRRVMGAGIAITlsSAGALSFCMALILltvcrniitllRETVIAQ 1068
Cdd:COG4097 3 RLRALLLIALYALLVLLPLLWLLADPLPAPAGGRGLRTALGQLTGLL--ALALMSLQFLLAA-----------RPPWLER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1069 YIP-FDSAIAFHKIVALFTLFWSTLHTIghcvnFYHVGtqsdRGLACLFQETFFGSDVVPTLSYWfyGTITGLTGIGLVI 1147
Cdd:COG4097 70 PFGgLDRLYRLHKWLGILALVLALAHPL-----LLLGP----KWLVGWGGLPARLAALLTLLRGL--AELLGEWAFYLLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1148 VMSIIYVFalpkftRRA--YHAFRLTHLLNIGFYALTILHGL---PSLFGSPKFGYYVVGPIVLFV---IDRIIG--LMQ 1217
Cdd:COG4097 139 ALVVLSLL------RRRlpYELWRLTHRLLAVAYLLLAFHHLllgGPFYWSPPAGVLWAALAAAGLaaaVYSRLGrpLRS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1218 YYKSLDIAHAEILPSDI--IYIEYRRPREFEYKSGQ--WITVSSPSISctfNESHAFSIASSP-QDENMKLYIKAVGPWT 1292
Cdd:COG4097 213 RRHPYRVESVEPEAGDVveLTLRPEGGRWLGHRAGQfaFLRFDGSPFW---EEAHPFSISSAPgGDGRLRFTIKALGDFT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1293 WKLRSelirsLNTGSPfplIHMKGPYGDgnqewMNYEVA------IMVGAGIGVTPYASTLVDLVQKTSSDsfhrvrcRK 1366
Cdd:COG4097 290 RRLGR-----LKPGTR---VYVEGPYGR-----FTFDRRdtaprqVWIAGGIGITPFLALLRALAARPGDQ-------RP 349
|
410 420 430
....*....|....*....|....*....|....*....
gi 17507545 1367 VYFLWVCSSHKNFEwFVDMLKNVENQAKPgiLETHIFVT 1405
Cdd:COG4097 350 VDLFYCVRDEEDAP-FLEELRALAARLAG--LRLHLVVS 385
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
1039-1183 |
8.77e-13 |
|
Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.
Pssm-ID: 426438 [Multi-domain] Cd Length: 121 Bit Score: 66.52 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1039 AGALSF-CMALILLTVCR-NIITLLRetviaqYIPFDSAIAFHKIVALFTLFWSTLHTIGHCVNFYHVGtqsdrglaclf 1116
Cdd:pfam01794 1 LGILALaLLPLLLLLALRnNPLEWLT------GLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFS----------- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17507545 1117 qetfFGSDVVPTLSYWFYgtitgLTGIGLVIVMSIIYVFALPKFTRRAYHAFRLTHLLNIGFYALTI 1183
Cdd:pfam01794 64 ----LEGILDLLLKRPYN-----ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
1233-1342 |
7.17e-05 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 46.01 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1233 DIIYIEYRRPRE-FEYKSGQWITVSSPSisctFNESHAFSIASSPQDEN-MKLYIKAVGPWTwklrsELIRSLNTGSpfp 1310
Cdd:COG0543 11 DVYLLRLEAPLIaLKFKPGQFVMLRVPG----DGLRRPFSIASAPREDGtIELHIRVVGKGT-----RALAELKPGD--- 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 17507545 1311 LIHMKGPYGDGnqewmnYEV------AIMVGAGIGVTP 1342
Cdd:COG0543 79 ELDVRGPLGNG------FPLedsgrpVLLVAGGTGLAP 110
|
|
| PTZ00183 |
PTZ00183 |
centrin; Provisional |
811-903 |
4.33e-03 |
|
centrin; Provisional
Pssm-ID: 185503 [Multi-domain] Cd Length: 158 Bit Score: 39.67 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 811 TISREELASAM---GMKANNEFVKRMFAMTAKHNEDSLSFNEFLTVL-REFVNAPQKQKLQTLFKMCDLEGKNKVLRKDL 886
Cdd:PTZ00183 33 TIDPKELKVAMrslGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMtKKLGERDPREEILKAFRLFDDDKTGKISLKNL 112
|
90
....*....|....*..
gi 17507545 887 AELVKSLnqtaGVHITE 903
Cdd:PTZ00183 113 KRVAKEL----GETITD 125
|
|
| EFh_PI-PLC |
cd15898 |
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
799-937 |
9.40e-03 |
|
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.
Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 38.03 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 799 SFDSSNDDILN-ETISReeLASAMGMKANNEFVKRMFAMTAKHNEDSLSFNEFLTVLREFVNAPQkqkLQTLFKMCDLEG 877
Cdd:cd15898 8 KADKDGDGKLSlKEIKK--LLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPE---LEPIFKKYAGTN 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17507545 878 KNKVlrkDLAELVKSLNQTAGVHITESVQLRLFNdvlhKSGVSDDAEYLTCNNF-DALFSE 937
Cdd:cd15898 83 RDYM---TLEEFIRFLREEQGENVSEEECEELIE----KYEPERENRQLSFEGFtNFLLSP 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| dual_peroxidase_like |
cd09820 |
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase ... |
41-596 |
0e+00 |
|
Dual oxidase and related animal heme peroxidases; Animal heme peroxidases of the dual-oxidase like subfamily play vital roles in the innate mucosal immunity of gut epithelia. They provide reactive oxygen species which help control infection.
Pssm-ID: 188652 [Multi-domain] Cd Length: 558 Bit Score: 936.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 41 YDGWYNNLANSEWGSAGSRLHRDARSYYSDGVYSVNNS-LPSARELSDILFKGESGIPNTRGCTTLLAFFSQVVAYEIMQ 119
Cdd:cd09820 1 YDGWYNNLAHPEWGAADSRLTRRLPAHYSDGVYAPSGEeRPNPRSLSNLLMKGESGLPSTRNRTALLVFFGQHVVSEILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 120 SNGVSCPLETLKIQVPLCDNVFDNECEGKTTIPFYRAKYDKATGNGLNSPREQINERTSWIDGSFIYGTTQPWVSALRSF 199
Cdd:cd09820 81 ASRPGCPPEYFNIEIPKGDPVFDPECTGNIELPFQRSRYDKNTGYSPNNPREQLNEVTSWIDGSSIYGSSKAWSDALRSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 200 KQGRLAEGV-PGYPPLNNPHIPLNNPAPPQVHRLMSPDRLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIYREHPDWT 278
Cdd:cd09820 161 SGGRLASGDdGGFPRRNTNRLPLANPPPPSYHGTRGPERLFKLGNPRGNENPFLLTFGILWFRYHNYLAQRIAREHPDWS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 279 DEQIFQAARRLVIASMQKIIAYDFVPGLLGEDVrlSNYTKYMPHVPPGISHAFGAAAFRFPHSIVPPAMLLRKRGNK-CE 357
Cdd:cd09820 241 DEDIFQEARKWVIATYQNIVFYEWLPALLGTNV--PPYTGYKPHVDPGISHEFQAAAFRFGHTLVPPGVYRRNRQCNfRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 358 FRTEVGGYPALRLCQNWWNAQDIVKEYSVDEIILGMASQIAERDDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGV 437
Cdd:cd09820 319 VLTTSGGSPALRLCNTYWNSQEPLLKSDIDELLLGMASQIAEREDNIIVEDLRDYLFGPLEFSRRDLMALNIQRGRDHGL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 438 PPYNELRRTFGLAP-KTWETMNEDFYKKHTAKVEKLKELYGGNILYLDAYVGGMLEGGENGPGEMFKEIIKDQFTRIRDG 516
Cdd:cd09820 399 PDYNTAREAFGLPPrTTWSDINPDLFKKDPELLERLAELYGNDLSKLDLYVGGMLESKGGGPGELFRAIILDQFQRLRDG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 517 DRFWFENKLNRLFTDEEVQMIHSITLRDIIKATTDIDETMLQKDVFFFKEGDPCPQPFQVNTIGLEPCAPLIQSTYWDDN 596
Cdd:cd09820 479 DRFWFENVKNGLFTAEEIEEIRNTTLRDVILAVTDIDNTDLQKNVFFWKNGDPCPQPKQLTENMLEPCTPLTVYDYFEGS 558
|
|
| An_peroxidase |
pfam03098 |
Animal haem peroxidase; |
39-562 |
1.82e-176 |
|
Animal haem peroxidase;
Pssm-ID: 460804 [Multi-domain] Cd Length: 531 Bit Score: 537.91 E-value: 1.82e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 39 QRYDGWYNNLANSEWGSAGSRLHRDARSYYSDGVY-----SVNNSLPSARELSDILFKGESGIPNTRgCTTLLAFFSQVV 113
Cdd:pfam03098 2 RTIDGSCNNLKNPSWGAAGTPFARLLPPAYEDGVSaprgsSSGSPLPSPRLVSNKLFAGDSGIPDPN-LTLLLMQWGQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 114 AYEIMQSNGVSCPLET---------------LKIQVPLCDNVFDNEceGKTTIPFYRAKYDKATGNglnsPREQINERTS 178
Cdd:pfam03098 81 DHDLTLTPESTSPNGSscdcccppenlhppcFPIPIPPDDPFFSPF--GVRCMPFVRSAPGCGLGN----PREQINQVTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 179 WIDGSFIYGTTQPWVSALRSFKQGRLAEGVP----GYPPLNNPHIPLNNPAPPQVhrlmspdrLFMLGDSRVNENPGLLS 254
Cdd:pfam03098 155 FLDGSQVYGSSEETARSLRSFSGGLLKVNRSddgkELLPFDPDGPCCCNSSGGVP--------CFLAGDSRANENPGLTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 255 FGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDV------RLSNYTKYMPHVPPGIS 328
Cdd:pfam03098 227 LHTLFLREHNRIADELAKLNPHWSDETLFQEARKIVIAQIQHITYNEWLPAILGEDNmnwfglLPLPYNGYDPNVDPSIS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 329 HAFGAAAFRFPHSIVPPAMLLRkrgNKCEFRTEvggyPALRLCQNWWNAQDIVkEYSVDEIILGMASQIAERDDNIVVED 408
Cdd:pfam03098 307 NEFATAAFRFGHSLIPPFLYRL---DENNVPEE----PSLRLHDSFFNPDRLY-EGGIDPLLRGLATQPAQAVDNNFTEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 409 LRDYIFGPM-HFSRLDVVASSIMRGRDNGVPPYNELRRTFGL-APKTWETMNEDFykkHTAKVEKLKELYgGNILYLDAY 486
Cdd:pfam03098 379 LTNHLFGPPgEFSGLDLAALNIQRGRDHGLPGYNDYREFCGLpPAKSFEDLTDVI---PNEVIAKLRELY-GSVDDIDLW 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507545 487 VGGMLEGGENG--PGEMFKEIIKDQFTRIRDGDRFWFENKLNRLFTDEEVQMIHSITLRDIIKATTDIDETMlQKDVF 562
Cdd:pfam03098 455 VGGLAEKPLPGglVGPTFACIIGDQFRRLRDGDRFWYENGNQGSFTPEQLEEIRKTSLARVICDNTDIIETI-QPNVF 531
|
|
| peroxinectin_like_bacterial |
cd09822 |
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are ... |
78-563 |
1.64e-106 |
|
Uncharacterized family of heme peroxidases, mostly bacterial; Animal heme peroxidases are diverse family of enzymes which are not restricted to animals. Members are also found in metazoans, fungi, and plants, and also in bacteria - like most members of this family of uncharacterized proteins.
Pssm-ID: 188654 [Multi-domain] Cd Length: 420 Bit Score: 345.45 E-value: 1.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 78 SLPSARELSDILFKGESGIPNTRGCTTLLAFFSQVVAYEIMQSNGvscpletlkiqvplcdnvfdnecegkttipfyrak 157
Cdd:cd09822 1 DRPSPREISNAVADQTESIPNSRGLSDWFWVWGQFLDHDIDLTPD----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 158 ydkatgnglnSPREQINERTSWIDGSFIYGTTQPWVSALRSFKQGRLAEGVP---GYPPLNNPHIPLNNPAPPqvhrlms 234
Cdd:cd09822 46 ----------NPREQINAITAYIDGSNVYGSDEERADALRSFGGGKLKTSVAnagDLLPFNEAGLPNDNGGVP------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 235 PDRLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDVrLS 314
Cdd:cd09822 109 ADDLFLAGDVRANENPGLTALHTLFVREHNRLADELARRNPSLSDEEIYQAARAIVIAEIQAITYNEFLPALLGENA-LP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 315 NYTKYMPHVPPGISHAFGAAAFRFPHSIVPPAMLlrkRGNkcEFRTEVGgypALRLCQNWWNAQDIVkEYSVDEIILGMA 394
Cdd:cd09822 188 AYSGYDETVNPGISNEFSTAAYRFGHSMLSSELL---RGD--EDGTEAT---SLALRDAFFNPDELE-ENGIDPLLRGLA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 395 SQIAERDDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNELRRTFGLAP-KTWETMNEDFykkhtAKVEKLK 473
Cdd:cd09822 259 SQVAQEIDTFIVDDVRNFLFGPPGAGGFDLAALNIQRGRDHGLPSYNQLREALGLPAvTSFSDITSDP-----DLAARLA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 474 ELYgGNILYLDAYVGGMLEGGENGP--GEMFKEIIKDQFTRIRDGDRFWFEnklNRLFTDEEVQMIHSITLRDIIKATTD 551
Cdd:cd09822 334 SVY-GDVDQIDLWVGGLAEDHVNGGlvGETFSTIIADQFTRLRDGDRFFYE---NDDLLLDEIADIENTTLADVIRRNTD 409
|
490
....*....|..
gi 17507545 552 IDetMLQKDVFF 563
Cdd:cd09822 410 VD--DIQDNVFL 419
|
|
| An_peroxidase_like |
cd05396 |
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes ... |
172-546 |
3.52e-88 |
|
Animal heme peroxidases and related proteins; A diverse family of enzymes, which includes prostaglandin G/H synthase, thyroid peroxidase, myeloperoxidase, linoleate diol synthase, lactoperoxidase, peroxinectin, peroxidasin, and others. Despite its name, this family is not restricted to metazoans: members are found in fungi, plants, and bacteria as well.
Pssm-ID: 188647 [Multi-domain] Cd Length: 370 Bit Score: 292.02 E-value: 3.52e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 172 QINERTSWIDGSFIYGTTQPWVSALRSFKQGRLAEGVPGYPPLNNPHIPLNNPAPPQVHRLMSPDRLFMLGDSRVNENPG 251
Cdd:cd05396 1 QLNARTPYLDGSSIYGSNPDVARALRTFKGGLLKTNEVKGPSYGTELLPFNNPNPSMGTIGLPPTRCFIAGDPRVNENLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 252 LLSFGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDVRLSN---YTKYMPHVPPGIS 328
Cdd:cd05396 81 LLAVHTLFLREHNRLADRLKKEHPEWDDERLYQEARLIVIAQYQLITYNEYLPAILGKFTDPRDdlvLLFPDPDVVPYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 329 HAFGAAAFRFPHSIVPPAMlLRKRGNkcefrTEVGGYPALRLCQNWWNAQD-IVKEYSVDEIILGMASQIAERDDNIVVE 407
Cdd:cd05396 161 SEFFTAAYRFGHSLVPEGV-DRIDEN-----GQPKEIPDVPLKDFFFNTSRsILSDTGLDPLLRGFLRQPAGLIDQNVDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 408 DlrDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNELRRTFGL-APKTWETMNedfykKHTAKVEKLKELYGG--NIlylD 484
Cdd:cd05396 235 V--MFLFGPLEGVGLDLAALNIQRGRDLGLPSYNEVRRFIGLkPPTSFQDIL-----TDPELAKKLAELYGDpdDV---D 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17507545 485 AYVGGMLEGGENG--PGEMFKEIIKDQFTRIRDGDRFWFENklNRLFTDEEV-QMIHSITLRDII 546
Cdd:cd05396 305 LWVGGLLEKKVPParLGELLATIILEQFKRLVDGDRFYYVN--YNPFGKSGKeELEKLISLADII 367
|
|
| peroxinectin_like |
cd09823 |
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a ... |
170-546 |
1.17e-84 |
|
peroxinectin_like animal heme peroxidases; Peroxinectin is an arthropod protein that plays a role in invertebrate immunity mechanisms. Specifically, peroxinectins are secreted as cell-adhesive and opsonic peroxidases. The immunity mechanism appears to involve an interaction between peroxinectin and a transmembrane receptor of the integrin family. Human myeloperoxidase, which is included in this wider family, has also been reported to interact with integrins.
Pssm-ID: 188655 [Multi-domain] Cd Length: 378 Bit Score: 282.16 E-value: 1.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 170 REQINERTSWIDGSFIYGTTQPWVSALRSFKQGRLAEGVPGypplNNPHIPLNNPAPPQVHRLMSPDRLFMLGDSRVNEN 249
Cdd:cd09823 1 REQLNQVTSFLDGSQVYGSSEEEARKLRTFKGGLLKTQRRN----GRELLPFSNNPTDDCSLSSAGKPCFLAGDGRVNEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 250 PGLLSFGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDV------RLSN---YTKYM 320
Cdd:cd09823 77 PGLTSMHTLFLREHNRIADELKKLNPHWDDERLFQEARKIVIAQMQHITYNEFLPILLGRELmekfglYLLTsgyFNGYD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 321 PHVPPGISHAFGAAAFRFPHSIVPPAM-LLRKRGNKCEFrtevggypaLRLCQNWWNAQDIVKEYSVDEIILGMASQIAE 399
Cdd:cd09823 157 PNVDPSILNEFAAAAFRFGHSLVPGTFeRLDENYRPQGS---------VNLHDLFFNPDRLYEEGGLDPLLRGLATQPAQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 400 R-DDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNELRRTFGL-APKTWETMNEDFYKKHtakVEKLKELYG 477
Cdd:cd09823 228 KvDRFFTDELTTHFFFRGGNPFGLDLAALNIQRGRDHGLPGYNDYREFCGLpRATTFDDLLGIMSPET---IQKLRRLYK 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17507545 478 --GNIlylDAYVGGMLE----GGENGPgeMFKEIIKDQFTRIRDGDRFWFENK-LNRLFTDEEVQMIHSITLRDII 546
Cdd:cd09823 305 svDDI---DLYVGGLSEkpvpGGLVGP--TFACIIGEQFRRLRRGDRFWYENGgQPSSFTPAQLNEIRKVSLARII 375
|
|
| peroxidasin_like |
cd09826 |
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted ... |
168-569 |
5.12e-74 |
|
Animal heme peroxidase domain of peroxidasin and related proteins; Peroxidasin is a secreted heme peroxidase which is involved in hydrogen peroxide metabolism and peroxidative reactions in the cardiovascular system. The domain co-occurs with extracellular matrix domains and may play a role in the formation of the extracellular matrix.
Pssm-ID: 188658 Cd Length: 440 Bit Score: 254.15 E-value: 5.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 168 SPREQINERTSWIDGSFIYGTTQPWVSALR--SFKQGRLAEGVPgyPPLNNPHIPLNNPAPPQVHR--LMSPDRLFMLGD 243
Cdd:cd09826 35 TPREQINQLTSYIDASNVYGSSDEEALELRdlASDRGLLRVGIV--SEAGKPLLPFERDSPMDCRRdpNESPIPCFLAGD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 244 SRVNENPGLLSFGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGED--VRLSNYTKYMP 321
Cdd:cd09826 113 HRANEQLGLTSMHTLWLREHNRIASELLELNPHWDGETIYHETRKIVGAQMQHITYSHWLPKILGPVgmEMLGEYRGYNP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 322 HVPPGISHAFGAAAFRFPHSIVPPAMllrKRGNKcEFRTEVGGYPALRlcQNWWNAQDIVKEYSVDEIILGM---ASQIA 398
Cdd:cd09826 193 NVNPSIANEFATAAFRFGHTLINPIL---FRLDE-DFQPIPEGHLPLH--KAFFAPYRLVNEGGIDPLLRGLfatAAKDR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 399 ERDDNIVVEdLRDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNELRRTFGL-APKTWETMNEDFykKHTAKVEKLKELYG 477
Cdd:cd09826 267 VPDQLLNTE-LTEKLFEMAHEVALDLAALNIQRGRDHGLPGYNDYRKFCNLsVAETFEDLKNEI--KNDDVREKLKRLYG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 478 --GNIlylDAYVGGMLE----GGENGPgeMFKEIIKDQFTRIRDGDRFWFENKlnRLFTDEEVQMIHSITLRDIIKATTD 551
Cdd:cd09826 344 hpGNI---DLFVGGILEdllpGARVGP--TLACLLAEQFRRLRDGDRFWYENP--GVFSPAQLTQIKKTSLARVLCDNGD 416
|
410
....*....|....*....
gi 17507545 552 -IDEtmLQKDVFFFKEGDP 569
Cdd:cd09826 417 nITR--VQEDVFLVPGNPH 433
|
|
| myeloperoxidase_like |
cd09824 |
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of ... |
161-573 |
1.39e-62 |
|
Myeloperoxidases, eosinophil peroxidases, and lactoperoxidases; This well conserved family of animal heme peroxidases contains members with somewhat diverse functions. Myeloperoxidases are lysosomal proteins found in azurophilic granules of neutrophils and the lysosomes of monocytes. They are involved in the formation of microbicidal agents upon activation of activated neutrophils (neutrophils undergoing respiratory bursts as a result of phagocytosis), by catalyzing the conversion of hydrogen peroxide to hypochlorous acid. As a heme protein, myeloperoxidase is responsible for the greenish tint of pus, which is rich in neutrophils. Eosinophil peroxidases are haloperoxidases as well, preferring bromide over chloride. Expressed by eosinophil granulocytes, they are involved in attacking multicellular parasites and play roles in various inflammatory diseases such as asthma. The haloperoxidase lactoperoxidase is secreted from mucosal glands and provides antibacterial activity by oxidizing a variety of substrates such as bromide or chloride in the presence of hydrogen peroxide.
Pssm-ID: 188656 [Multi-domain] Cd Length: 411 Bit Score: 219.98 E-value: 1.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 161 ATGNGLNSPREQINERTSWIDGSFIYGTTQPWVSALR--SFKQGRLA-------EGVPgYPPLNNPHiplNNPAPPQVHR 231
Cdd:cd09824 3 GACTSKRNVREQINALTSFVDASMVYGSEPSLAK*LRnlTNQLGLLAvnqrftdNGLA-LLPFENLH---NDPCALRNTS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 232 LMSPdrLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDV 311
Cdd:cd09824 79 ANIP--CFLAGDTRVSENPGLAALHTLLLREHNRLARELHRLNPHWDGETLYQEARKIVGAMVQIITYRDYLPLILGEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 312 --RLSNYTKYMPHVPPGISHAFgAAAFRFPHSIVPPAMllrkrgnkceFR-----TEVGGYPALRLCQNWWNAQDIVKEY 384
Cdd:cd09824 157 aaRLPPYRGYNESVDPRIANVF-TTAFRRGHTTVQPFV----------FRldenyQPHPPNPQVPLHKAFFASWRIIREG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 385 SVDEIILGMASQIAE--RDDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNELRRTFGL-APKTWETMNEDF 461
Cdd:cd09824 226 GIDPILRGLMATPAKlnNQNQMLVDELRERLFQQTKRMGLDLAALNLQRGRDHGLPGYNAWRRFCGLsQPQNLAELAAVL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 462 YKKHTAKveKLKELYGG--NIlylDAYVGG----MLEGGENGPgeMFKEIIKDQFTRIRDGDRFWFENklNRLFTDEEVQ 535
Cdd:cd09824 306 NNTVLAR--KLLDLYGTpdNI---DIWIGGvaepLVPGGRVGP--LLACLISRQFRRIRDGDRFWWEN--PGVFTEEQRE 376
|
410 420 430
....*....|....*....|....*....|....*...
gi 17507545 536 MIHSITLRDIIKATTDIdeTMLQKDVFFfkegdPCPQP 573
Cdd:cd09824 377 SLRSVSLSRIICDNTGI--TKVPRDPFQ-----PNSYP 407
|
|
| thyroid_peroxidase |
cd09825 |
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is ... |
78-566 |
1.70e-50 |
|
Thyroid peroxidase (TPO); TPO is a member of the animal heme peroxidase family, which is expressed in the thyroid and involved in the processing of iodine and iodine compounds. Specifically, TPO oxidizes iodide via hydrogen peroxide to form active iodine, which is then, for example, incorporated into the tyrosine residues of thyroglobulin to yield mono- and di-iodotyrosines.
Pssm-ID: 188657 [Multi-domain] Cd Length: 565 Bit Score: 189.18 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 78 SLPSARELS-DILFKGESGIPNTRGCTTLLAFFSQVVAYEI---MQSNGVSCPLETLKIQVPlCDNVF----------DN 143
Cdd:cd09825 35 TLPSVREVSnKIMRTSSTAVTPDDLYSHMLTVWGQYIDHDIdftPQSVSRTMFIGSTDCKMT-CENQNpcfpiqlpseDP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 144 ECEGKTTIPFYRAKYDKATGNG--------LNSPREQINERTSWIDGSFIYGTTQPWVSALRSFKQG----RLAEGVPG- 210
Cdd:cd09825 114 RILGRACLPFFRSSAVCGTGDTstlfgnlsLANPREQINGLTSFIDASTVYGSTLALARSLRDLSSDdgllRVNSKFDDs 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 211 ---YPPLNNPHIPLNNPAPPQVHRlmSPdrLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIYREHPDWTDEQIFQAAR 287
Cdd:cd09825 194 grdYLPFQPEEVSSCNPDPNGGER--VP--CFLAGDGRASEVLTLTASHTLWLREHNRLARALKSINPHWDGEQIYQEAR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 288 RLVIASMQKIIAYDFVPGLLGE---DVRLSNYTKYMPHVPPGISHAFGAAAFRFPHSIVPPamLLRKRGNKCEFRTEVGG 364
Cdd:cd09825 270 KIVGALHQIITFRDYIPKILGPeafDQYGGYYEGYDPTVNPTVSNVFSTAAFRFGHATIHP--TVRRLDENFQEHPVLPN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 365 YPALRLCQNWWNaqdIVKEYSVDEIILGMASQIAE--RDDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNE 442
Cdd:cd09825 348 LALHDAFFSPWR---LVREGGLDPVIRGLIGGPAKlvTPDDLMNEELTEKLFVLSNSSTLDLASLNLQRGRDHGLPGYND 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 443 LRRTFGLAPKTWETMNEDFYKKHtAKVEKLKELYG--GNIlylDAYVGGMLEGGENG--PGEMFKEIIKDQFTRIRDGDR 518
Cdd:cd09825 425 WREFCGLPRLATPADLATAIADQ-AVADKILDLYKhpDNI---DVWLGGLAEDFLPGarTGPLFACLIGKQMKALRDGDR 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 17507545 519 FWFENklNRLFTDEEVQMIHSITLRDIIKATTDIdeTMLQKDVFFFKE 566
Cdd:cd09825 501 FWWEN--SNVFTDAQRRELRKHSLSRVICDNTGL--TRVPPDAFQLGK 544
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
1224-1408 |
1.89e-42 |
|
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.
Pssm-ID: 99783 [Multi-domain] Cd Length: 210 Bit Score: 154.77 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1224 IAHAEILP-SDIIYIEYRRPREFEYKSGQWITVSSPSISCTFnESHAFSIASSPQDEN--MKLYIKAV-GPWTwKLRSEL 1299
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLLSFW-QSHPFTIASSPEDEQdtLSLIIRAKkGFTT-RLLRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1300 IRSLNTGSPFPlIHMKGPYGDGNQEWMNYEVAIMVGAGIGVTPYASTLVDLVQKTSSdsfhRVRCRKVYFLWVCSSHKNF 1379
Cdd:cd06186 79 LKSPGGGVSLK-VLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSK----TSRTRRVKLVWVVRDREDL 153
|
170 180 190
....*....|....*....|....*....|..
gi 17507545 1380 EWFVDML---KNVENQAkpgilETHIFVTQMF 1408
Cdd:cd06186 154 EWFLDELraaQELEVDG-----EIEIYVTRVV 180
|
|
| An_peroxidase_bacterial_2 |
cd09821 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
161-562 |
2.62e-28 |
|
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.
Pssm-ID: 188653 [Multi-domain] Cd Length: 570 Bit Score: 122.14 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 161 ATGNGLNSPREQINERTSWIDGSFIYGTTQPWVSALRSFK-----QGRLAEG--------------------VPGYPPLN 215
Cdd:cd09821 72 GILGTADGEGEHTNVTTPFVDQNQTYGSHASHQVFLREYDgdgvaTGRLLEGatggsartghaflddiahnaAPKGGLGS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 216 NPHIPLNNPAPPQVHRLMSPDRL---FMLGDSRVNENPGLLSFGLILFRWHN----------------YNANQIYREHPD 276
Cdd:cd09821 152 LRDNPTEDPPGPGAPGSYDNELLdahFVAGDGRVNENIGLTAVHTVFHREHNrlvdqikdtllqsadlAFANEAGGNNLA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 277 WTDEQIFQAARRLVIASMQKIIAYDF---VPGLLGEDVRLSNYTkymPHVPPGISHAFGAAAFRFPHSIVPPAMLLRKRG 353
Cdd:cd09821 232 WDGERLFQAARFANEMQYQHLVFEEFarrIQPGIDGFGSFNGYN---PEINPSISAEFAHAVYRFGHSMLTETVTRIGPD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 354 NKCEFRTEVGGYPALrLCQNWWNAQDIVKEYSVDEIILGMASQIAERDDNIVVEDLRDYIFG-PmhfsrLDVVASSIMRG 432
Cdd:cd09821 309 ADEGLDNQVGLIDAF-LNPVAFLPATLYAEEGAGAILRGMTRQVGNEIDEFVTDALRNNLVGlP-----LDLAALNIARG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 433 RDNGVPPYNELRR--------TFGLAPKT-WETMN---------EDFYK--KHTAKVEKLKELYGG------NILYLDA- 485
Cdd:cd09821 383 RDTGLPTLNEARAqlfaatgdTILKAPYEsWNDFGarlknpeslINFIAayGTHLTITGATTLAAKraaaqdLVDGGDGa 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 486 --------------------------YVGGMLEGGENGPGEM---FKEIIKDQFTRIRDGDRFWFENKLNRLFTDEEvqm 536
Cdd:cd09821 463 padradfmnaagagagtvkgldnvdlWVGGLAEKQVPFGGMLgstFNFVFEEQMDRLQDGDRFYYLSRTAGLDLLNQ--- 539
|
490 500
....*....|....*....|....*.
gi 17507545 537 IHSITLRDIIKATTDIdeTMLQKDVF 562
Cdd:cd09821 540 LENNTFADMIMRNTGA--THLPQDIF 563
|
|
| PIOX_like |
cd09818 |
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family ... |
169-492 |
2.52e-25 |
|
Animal heme oxidases similar to plant pathogen-inducible oxygenases; This is a diverse family of oxygenases related to the animal heme peroxidases, with members from plants, animals, and bacteria. The plant pathogen-inducible oxygenases (PIOX) oxygenate fatty acids into 2R-hydroperoxides. They may be involved in the hypersensitive reaction, rapid and localized cell death induced by infection with pathogens, and the rapidly induced expression of PIOX may be caused by the oxidative burst that occurs in the process of cell death.
Pssm-ID: 188650 [Multi-domain] Cd Length: 484 Bit Score: 111.61 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 169 PREQINERTSWIDGSFIYGTTQPWVSALRSFKQ-GRLAEGVPGYPPLnnphIPLNNpappqvhrlmspdrlfmLGDSRVN 247
Cdd:cd09818 83 PPTYINTNTHWWDGSQIYGSTEEAQKRLRTFPPdGKLKLDADGLLPV----DEHTG-----------------LPLTGFN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 248 ENpglLSFGLILF-----RWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVP-----------------G 305
Cdd:cd09818 142 DN---WWVGLSLLhtlfvREHNAICDALRKEYPDWSDEQLFDKARLVNAALMAKIHTVEWTPailahptleiamranwwG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 306 LLGEDVRlsnytKYMPHVppGISHA-----------FGA---------AAFRfPHSIVPpamllrkrgNKCEFRTEVGGY 365
Cdd:cd09818 219 LLGERLK-----RVLGRD--GTSELlsgipgsppnhHGVpyslteefvAVYR-MHPLIP---------DDIDFRSADDGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 366 palrlcqnwwnaqdIVKEYSVDEIILGMASqiaERDDNIVVEDLRdYIFG------------P---MHFSR-----LDVV 425
Cdd:cd09818 282 --------------TGEEISLTDLAGGKAR---ELLRKLGFADLL-YSFGithpgaltlhnyPrflRDLHRpdgrvIDLA 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507545 426 ASSIMRGRDNGVPPYNELRRTFGLAP-KTWETMNEDfykKHTAkvEKLKELYGGNILYLDAYVGGMLE 492
Cdd:cd09818 344 AIDILRDRERGVPRYNEFRRLLHLPPaKSFEDLTGD---EEVA--AELREVYGGDVEKVDLLVGLLAE 406
|
|
| prostaglandin_endoperoxide_synthase |
cd09816 |
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal ... |
79-492 |
2.54e-22 |
|
Animal prostaglandin endoperoxide synthase and related bacterial proteins; Animal prostaglandin endoperoxide synthases, including prostaglandin H2 synthase and a set of similar bacterial proteins which may function as cyclooxygenases. Prostaglandin H2 synthase catalyzes the synthesis of prostaglandin H2 from arachidonic acid. In two reaction steps, arachidonic acid is converted to Prostaglandin G2, a peroxide (cyclooxygenase activity) and subsequently converted to the end product via the enzyme's peroxidase activity. Prostaglandin H2 synthase is the target of aspirin and other non-steroid anti-inflammatory drugs such as ibuprofen, which block the substrate's access to the active site and may acetylate a conserved serine residue. In humans and other mammals, prostaglandin H2 synthase (PGHS), also called cyclooxygenase (COX) is present as at least two isozymes, PGHS-1 (or COX-1) and PGHS-2 (or COX-2), respectively. PGHS-1 is expressed constitutively in most mammalian cells, while the expression of PGHS-2 is induced via inflammation response in endothelial cells, activated macrophages, and others. COX-3 is a splice variant of COX-1.
Pssm-ID: 188648 [Multi-domain] Cd Length: 490 Bit Score: 102.73 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 79 LPSARELSDILFKGESGIPNTRGCTTLLAFFSQVVAYEimqsngvscpletlkiqvplcdnvfdnecegkttipFYRAKY 158
Cdd:cd09816 76 LPDVEELAELFLRRREFIPDPQKTTLLFPFFAQWFTDQ------------------------------------FLRTDP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 159 DKATGNGLNSPreqinertswIDGSFIYGTTQPWVSALRSFKQGRL-AEGVPG--YPPL------NNPHIPLNNPAPPQV 229
Cdd:cd09816 120 GDPRRNTSNHG----------IDLSQIYGLTEARTHALRLFKDGKLkSQMINGeeYPPYlfedggVKMEFPPLVPPLGDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 230 HRLMSPDRLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGE 309
Cdd:cd09816 190 LTPEREAKLFAVGHERFNLTPGLFMLNTIWLREHNRVCDILKKEHPDWDDERLFQTARNILIGELIKIVIEDYINHLSPY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 310 DVRLSnytkymphVPPGIshAFG---------AAAFRFP---HSIVPPAMLLR-KRGNKCEFRtevggypalrlcqnwWN 376
Cdd:cd09816 270 HFKLF--------FDPEL--AFNepwqrqnriALEFNLLyrwHPLVPDTFNIGgQRYPLSDFL---------------FN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 377 AqDIVKEYSVDEIILGMASQIAERddnivvedlrdyiFGPMHFSR--LDVVASSIMRGRDNGVPPYNELRRTFGLAP-KT 453
Cdd:cd09816 325 N-DLVVDHGLGALVDAASRQPAGR-------------IGLRNTPPflLPVEVRSIEQGRKLRLASFNDYRKRFGLPPyTS 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 17507545 454 WETMNEDfykkhTAKVEKLKELYgGNILYLDAYVGGMLE 492
Cdd:cd09816 391 FEELTGD-----PEVAAELEELY-GDVDAVEFYVGLFAE 423
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
1328-1484 |
1.94e-20 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 89.32 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1328 YEVAIMVGAGIGVTPYASTLVDLVQKTSSDsfhrvRCRKVYFLWVCSSHKNFEWFVDMLKNVENQaKPGILETHIFVTQM 1407
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKKL-----KTKKIKFYWVVRDLSSLEWFKDVLNELEEL-KELNIEIHIYLTGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1408 fhkfdlrttmlYICEKHFRATNSGIS--MFTGLHAKN--------HFGRPNFKAFFQFIQSEHKEQSeIGVFSCGPVNLN 1477
Cdd:pfam08030 75 -----------YEAEDASDQSDSSIRseNFDSLMNEVigvdfvefHFGRPNWKEVLKDIAKQHPNGS-IGVFSCGPPSLV 142
|
....*..
gi 17507545 1478 ESIAEGC 1484
Cdd:pfam08030 143 DELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
1045-1406 |
3.61e-18 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 90.68 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1045 CMALILLTVcrniitlLRETVIAQY--IPFDSAIAFHKIVALFTLFWSTLH--------TIGHcvnfyHVGTQSDRglac 1114
Cdd:PLN02844 166 CLALLLLPV-------LRGLALFRLlgIQFEASVRYHVWLGTSMIFFATVHgastlfiwGISH-----HIQDEIWK---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1115 lFQETFfgsdvvptlSYWFYGTITGLTGIglvivmsIIYVFALPKFTRRAYHAFRLTHLLNIGFYALTILHGlpslfGSP 1194
Cdd:PLN02844 230 -WQKTG---------RIYLAGEIALVTGL-------VIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHA-----GDR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1195 KFgYYVVGPIVLFVIDRIIGLMQYYKSLDIAHAEILPSDIIYIEYRRPREFEYKSGQWITVSSPSIScTFnESHAFSIAS 1274
Cdd:PLN02844 288 HF-YMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSIS-RF-QWHPFSITS 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1275 SPQ--DENMKLYIKAVGPWTWKLRSELIRSLNTGSP----FPlIHMKGPYGDGNQEWMNYEVAIMVGAGIGVTPYASTLV 1348
Cdd:PLN02844 365 SSNidDHTMSVIIKCEGGWTNSLYNKIQAELDSETNqmncIP-VAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILK 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1349 DLVQKTSSdsfhRVRC-RKVYFLWVCSSHKNFEWFVDMLKNVENQAKPGI-LETHIFVTQ 1406
Cdd:PLN02844 444 EIASQSSS----RYRFpKRVQLIYVVKKSQDICLLNPISSLLLNQSSNQLnLKLKVFVTQ 499
|
|
| PLN02283 |
PLN02283 |
alpha-dioxygenase |
153-546 |
1.27e-17 |
|
alpha-dioxygenase
Pssm-ID: 177921 [Multi-domain] Cd Length: 633 Bit Score: 88.67 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 153 FYRAKYDKATGNGLNSprEQINERTSWIDGSFIYGTTQPWVSALRSFKQGRLAEGVPGYPPLNNPHIPLNnpappqvhrl 232
Cdd:PLN02283 189 FYKTKEVPTGSPDIKT--GSLNIRTPWWDGSVIYGSNEKGLRRVRTFKDGKLKISEDGLLLHDEDGIPIS---------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 233 mspdrlfmlGDSRvNENPGLLSFGLILFRWHNYNANQIYREHPDWTDEQIFQAARRLVIASMQKIIAYDFVP-------- 304
Cdd:PLN02283 257 ---------GDVR-NSWAGVSLLQALFVKEHNAVCDALKEEYPDFDDEELYRHARLVTSAVIAKIHTIDWTVellktdtl 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 305 ---------GLLGEDVR-------------LSNYTKYMPH-VPPGISHAFgAAAFRFpHSIVPPAMLLRkrgnkcefrtE 361
Cdd:PLN02283 327 lagmranwyGLLGKKFKdtfghiggpilsgLVGLKKPNNHgVPYSLTEEF-TSVYRM-HSLLPDHLILR----------D 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 362 VGGYPALRLCQnwwnaqDIVKEYSVDEII----------LGMASQIAE------------------RDdnIVVEDlRDYI 413
Cdd:PLN02283 395 ITAAPGENKSP------PLIEEIPMPELIglkgekklskIGFEKLMVSmghqacgalelwnypswmRD--LVPQD-IDGE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 414 FGPMHfsrLDVVASSIMRGRDNGVPPYNELRRTFGLAP-KTWETMNEDfykkhTAKVEKLKELYGGNILYLDAYVGGMLE 492
Cdd:PLN02283 466 DRPDH---VDMAALEIYRDRERGVARYNEFRRNLLMIPiSKWEDLTDD-----EEAIEVLREVYGDDVEKLDLLVGLMAE 537
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 17507545 493 ggENGPGEMFKEIIKDQF----TRIRDGDRFWFENKLNRLFTDEEVQMIHSI-TLRDII 546
Cdd:PLN02283 538 --KKIKGFAISETAFFIFllmaSRRLEADRFFTSNFNEKTYTKKGLEWVNTTeSLKDVI 594
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
989-1405 |
3.14e-17 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 86.10 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 989 TYRQHVFIIFCFVAINIVLFFELFWHSRYLNEDRDLRRVMGAGIAITlsSAGALSFCMALILltvcrniitllRETVIAQ 1068
Cdd:COG4097 3 RLRALLLIALYALLVLLPLLWLLADPLPAPAGGRGLRTALGQLTGLL--ALALMSLQFLLAA-----------RPPWLER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1069 YIP-FDSAIAFHKIVALFTLFWSTLHTIghcvnFYHVGtqsdRGLACLFQETFFGSDVVPTLSYWfyGTITGLTGIGLVI 1147
Cdd:COG4097 70 PFGgLDRLYRLHKWLGILALVLALAHPL-----LLLGP----KWLVGWGGLPARLAALLTLLRGL--AELLGEWAFYLLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1148 VMSIIYVFalpkftRRA--YHAFRLTHLLNIGFYALTILHGL---PSLFGSPKFGYYVVGPIVLFV---IDRIIG--LMQ 1217
Cdd:COG4097 139 ALVVLSLL------RRRlpYELWRLTHRLLAVAYLLLAFHHLllgGPFYWSPPAGVLWAALAAAGLaaaVYSRLGrpLRS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1218 YYKSLDIAHAEILPSDI--IYIEYRRPREFEYKSGQ--WITVSSPSISctfNESHAFSIASSP-QDENMKLYIKAVGPWT 1292
Cdd:COG4097 213 RRHPYRVESVEPEAGDVveLTLRPEGGRWLGHRAGQfaFLRFDGSPFW---EEAHPFSISSAPgGDGRLRFTIKALGDFT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1293 WKLRSelirsLNTGSPfplIHMKGPYGDgnqewMNYEVA------IMVGAGIGVTPYASTLVDLVQKTSSDsfhrvrcRK 1366
Cdd:COG4097 290 RRLGR-----LKPGTR---VYVEGPYGR-----FTFDRRdtaprqVWIAGGIGITPFLALLRALAARPGDQ-------RP 349
|
410 420 430
....*....|....*....|....*....|....*....
gi 17507545 1367 VYFLWVCSSHKNFEwFVDMLKNVENQAKPgiLETHIFVT 1405
Cdd:COG4097 350 VDLFYCVRDEEDAP-FLEELRALAARLAG--LRLHLVVS 385
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
1224-1319 |
4.60e-17 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 78.15 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1224 IAHAEILPSDIIYIEYRRP-REFEYKSGQWITVS-SPSISctFNESHAFSIASSPQDENMKLYIKAVGPWTWKLRSELIR 1301
Cdd:pfam08022 6 KAKVALLPDNVLKLRVSKPkKPFKYKPGQYMFINfLPPLS--FLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYLSS 83
|
90 100
....*....|....*....|..
gi 17507545 1302 S----LNTGSPFPLIHMKGPYG 1319
Cdd:pfam08022 84 ScpksPENGKDKPRVLIEGPYG 105
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
1135-1358 |
9.61e-16 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 82.61 E-value: 9.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1135 GTITGLTGIglvivmsIIYVFALPKFTRRAYHAFRLTHLLNIGFYALTILH-GLP-SLFGSPkfGYYVvgpivlFVIDRI 1212
Cdd:PLN02292 253 GEIALVAGL-------VMWATTYPKIRRRFFEVFFYTHYLYIVFMLFFVFHvGISfALISFP--GFYI------FLVDRF 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1213 IGLMQYYKSLDIAHAEILPSDIIYIEYRRPREFEYKSGQWITVSSPSISCTfnESHAFSIASSPQDENMKL--YIKAVGP 1290
Cdd:PLN02292 318 LRFLQSRNNVKLVSARVLPCDTVELNFSKNPMLMYSPTSIMFVNIPSISKL--QWHPFTITSSSKLEPEKLsvMIKSQGK 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507545 1291 WTWKLRSELIRSLNTGSPfpLIHMKGPYGDGNQEWMNYEVAIMVGAGIGVTPYASTLVDLVQKTSSDS 1358
Cdd:PLN02292 396 WSTKLYHMLSSSDQIDRL--AVSVEGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLIYTSSTET 461
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
1127-1358 |
1.62e-15 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 82.01 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1127 PTLSYWFYGTITGLTGIGLvivmsiiYVFALPKFTRRAYHAFRLTHLLNIGFYALTILHGLPSLFgspkfgYYVVGPIVL 1206
Cdd:PLN02631 228 PTYVPNLAGTIAMVIGIAM-------WVTSLPSFRRKKFELFFYTHHLYGLYIVFYVIHVGDSWF------CMILPNIFL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1207 FVIDRIIGLMQYYKSLDIAHAEILPSDIIYIEYRRPREFEYKSGQWITVSSPSISCTfnESHAFSIASSP--QDENMKLY 1284
Cdd:PLN02631 295 FFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKL--QWHPFTITSSSnlEKDTLSVV 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17507545 1285 IKAVGPWTWKLRSELIRSLNTGSpfplIHMKGPYGDGNQEWMNYEVAIMVGAGIGVTPYASTLVDLVQKTSSDS 1358
Cdd:PLN02631 373 IRRQGSWTQKLYTHLSSSIDSLE----VSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELIFQSQNPS 442
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
1228-1407 |
1.52e-14 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 74.41 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1228 EILPSDIIYIEYRRPREFEYKSGQWITVSSPSISCtfNESHAFSIASSPQDEN-MKLYIKAV--GPWTWKLRSELIRSLn 1304
Cdd:cd00322 4 EDVTDDVRLFRLQLPNGFSFKPGQYVDLHLPGDGR--GLRRAYSIASSPDEEGeLELTVKIVpgGPFSAWLHDLKPGDE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1305 tgspfplIHMKGPYGDGNQEWMNYEVAIMVGAGIGVTPYASTLVDLVQKTSSdsfhrvrcRKVYFLWVCsSHKNFEWFVD 1384
Cdd:cd00322 81 -------VEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG--------GEITLLYGA-RTPADLLFLD 144
|
170 180
....*....|....*....|...
gi 17507545 1385 MLKNVENqaKPGILETHIFVTQM 1407
Cdd:cd00322 145 ELEELAK--EGPNFRLVLALSRE 165
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
1039-1183 |
8.77e-13 |
|
Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.
Pssm-ID: 426438 [Multi-domain] Cd Length: 121 Bit Score: 66.52 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1039 AGALSF-CMALILLTVCR-NIITLLRetviaqYIPFDSAIAFHKIVALFTLFWSTLHTIGHCVNFYHVGtqsdrglaclf 1116
Cdd:pfam01794 1 LGILALaLLPLLLLLALRnNPLEWLT------GLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFS----------- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17507545 1117 qetfFGSDVVPTLSYWFYgtitgLTGIGLVIVMSIIYVFALPKFTRRAYHAFRLTHLLNIGFYALTI 1183
Cdd:pfam01794 64 ----LEGILDLLLKRPYN-----ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| An_peroxidase_bacterial_1 |
cd09819 |
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse ... |
166-453 |
2.81e-11 |
|
Uncharacterized bacterial family of heme peroxidases; Animal heme peroxidases are diverse family of enzymes which are not restricted to metazoans; members are also found in fungi, and plants, and in bacteria - like this family of uncharacterized proteins.
Pssm-ID: 188651 Cd Length: 465 Bit Score: 67.75 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 166 LNSPREQINERTSWIDGSFIYG---TTQPwvsALRSFKqgrlAEGVPGYPPLNNPHIPLNNPAPPQVHR--LMSPDRLFM 240
Cdd:cd09819 73 QIDPAELRNFRTPALDLDSVYGggpDGSP---YLYDQA----TPNDGAKLRVGRESPGGPGGLPGDGARdlPRNGQGTAL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 241 LGDSRVNENPGLLSFGLILFRWHNYNANQIYREHPDWtdEQIFQAARRLVIASMQKIIAYDFVPGLLGEDV------RLS 314
Cdd:cd09819 146 IGDPRNDENLIVAQLHLAFLRFHNAVVDALRAHGTPG--DELFEEARRLVRWHYQWLVLNDFLPRICDPDVvddvlaNGR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 315 NYTKYMPHVPPGISHAFGAAAFRFPHSIVPPAMLLRKRGNKCEFR-----TEVGGYPALR---LCQNWWnaqdivkeysV 386
Cdd:cd09819 224 RFYRFFREGKPFMPVEFSVAAYRFGHSMVRASYDYNRNFPDASLEllftfTGGGEGDLGGfspLPENWI----------I 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17507545 387 D-----EIILGMASQIAERDDNIVVEDLRDYIFGPMHFSRLDV--VASSIMRGRDNGVPPYNELRRTFGLAPKT 453
Cdd:cd09819 294 DwrrffDIDGSAPPQFARKIDTKLAPPLFDLPNGGVGLAPPMKslAFRNLLRGYRLGLPSGQAVARALGIAPLT 367
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
1228-1363 |
2.56e-09 |
|
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99795 [Multi-domain] Cd Length: 216 Bit Score: 58.81 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1228 EILPSDIIYIEYRRPrEFEYKSGQ--WITVSSPSISctfnESHAFSIASSPQDENM-KLYIKAVGPWTwklrSELIRSLN 1304
Cdd:cd06198 5 EVRPTTTLTLEPRGP-ALGHRAGQfaFLRFDASGWE----EPHPFTISSAPDPDGRlRFTIKALGDYT----RRLAERLK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17507545 1305 TGSPfplIHMKGPYGDgnqewMNYEVA----IMVGAGIGVTPYASTLVDLVQKTSSDS---FHRVR 1363
Cdd:cd06198 76 PGTR---VTVEGPYGR-----FTFDDRrarqIWIAGGIGITPFLALLEALAARGDARPvtlFYCVR 133
|
|
| FNR1 |
cd06195 |
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
1239-1350 |
4.09e-06 |
|
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99792 [Multi-domain] Cd Length: 241 Bit Score: 49.87 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1239 YRRPREFEYKSGQWITVSSPsisctfNESH-----AFSIASSPQDENMKLYIKAV--GPWTWKLrseliRSLNTGSPfpl 1311
Cdd:cd06195 17 VTRDIPFRFQAGQFTKLGLP------NDDGklvrrAYSIASAPYEENLEFYIILVpdGPLTPRL-----FKLKPGDT--- 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17507545 1312 IHM-KGPYG--------DGNQEWmnyevaiMVGAGIGVTPYASTLVDL 1350
Cdd:cd06195 83 IYVgKKPTGfltldevpPGKRLW-------LLATGTGIAPFLSMLRDL 123
|
|
| phenol_2-monooxygenase_like |
cd06211 |
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
1227-1353 |
4.89e-05 |
|
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.
Pssm-ID: 99807 Cd Length: 238 Bit Score: 46.55 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1227 AEILPSDI--IYIEYRRPREFEYKSGQWITVSSPSISCTfnesHAFSIASSPQDEN-MKLYIKAV--GPWTwklrSELIR 1301
Cdd:cd06211 14 IEDLTPTIkgVRLKLDEPEEIEFQAGQYVNLQAPGYEGT----RAFSIASSPSDAGeIELHIRLVpgGIAT----TYVHK 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17507545 1302 SLNTGSPfplIHMKGPYGDGNQEWMNYEVAIMVGAGIGVTPYASTLVDLVQK 1353
Cdd:cd06211 86 QLKEGDE---LEISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDLLER 134
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
1233-1342 |
7.17e-05 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 46.01 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1233 DIIYIEYRRPRE-FEYKSGQWITVSSPSisctFNESHAFSIASSPQDEN-MKLYIKAVGPWTwklrsELIRSLNTGSpfp 1310
Cdd:COG0543 11 DVYLLRLEAPLIaLKFKPGQFVMLRVPG----DGLRRPFSIASAPREDGtIELHIRVVGKGT-----RALAELKPGD--- 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 17507545 1311 LIHMKGPYGDGnqewmnYEV------AIMVGAGIGVTP 1342
Cdd:COG0543 79 ELDVRGPLGNG------FPLedsgrpVLLVAGGTGLAP 110
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
1243-1360 |
2.25e-04 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 44.39 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1243 REFEYKSGQWITVSSPsisctFNESH---AFSIASSPQDENMKLYIKAV--GPWTwklrSELIRSLNTGSPfplIHMKGP 1317
Cdd:COG1018 30 PLPRFRPGQFVTLRLP-----IDGKPlrrAYSLSSAPGDGRLEITVKRVpgGGGS----NWLHDHLKVGDT---LEVSGP 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17507545 1318 YGDgnqewMNYEVA-----IMVGAGIGVTPYASTLVDLVQKTSSDSFH 1360
Cdd:COG1018 98 RGD-----FVLDPEparplLLIAGGIGITPFLSMLRTLLARGPFRPVT 140
|
|
| monooxygenase_like |
cd06212 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
1224-1353 |
4.14e-04 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.
Pssm-ID: 99808 [Multi-domain] Cd Length: 232 Bit Score: 43.47 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1224 IAHAEILPSDIIYIEYR--RPREFEYKSGQWITVSSPSISctfnESHAFSIASSPQDE-NMKLYIKAV--GPWTWKLRSE 1298
Cdd:cd06212 5 VVAVEALTHDIRRLRLRleEPEPIKFFAGQYVDITVPGTE----ETRSFSMANTPADPgRLEFIIKKYpgGLFSSFLDDG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 17507545 1299 lirsLNTGSPfplIHMKGPYGDGNQEWMNYEVAIMVGAGIGVTPYASTLVDLVQK 1353
Cdd:cd06212 81 ----LAVGDP---VTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAAS 128
|
|
| FNR_iron_sulfur_binding_1 |
cd06215 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
1242-1363 |
3.98e-03 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99811 [Multi-domain] Cd Length: 231 Bit Score: 40.65 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 1242 PREFEYKSGQWITVSSPsISCTfNESHAFSIASSPQDEN-MKLYIKAVGP-----WtwklrseLIRSLNTGSPfplIHMK 1315
Cdd:cd06215 23 GSLFAYKPGQFLTLELE-IDGE-TVYRAYTLSSSPSRPDsLSITVKRVPGglvsnW-------LHDNLKVGDE---LWAS 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17507545 1316 GPYGDGN-QEWMNYEVAiMVGAGIGVTPYAS---TLVDLVQKTSSDSFHRVR 1363
Cdd:cd06215 91 GPAGEFTlIDHPADKLL-LLSAGSGITPMMSmarWLLDTRPDADIVFIHSAR 141
|
|
| PTZ00183 |
PTZ00183 |
centrin; Provisional |
811-903 |
4.33e-03 |
|
centrin; Provisional
Pssm-ID: 185503 [Multi-domain] Cd Length: 158 Bit Score: 39.67 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507545 811 TISREELASAM---GMKANNEFVKRMFAMTAKHNEDSLSFNEFLTVL-REFVNAPQKQKLQTLFKMCDLEGKNKVLRKDL 886
Cdd:PTZ00183 33 TIDPKELKVAMrslGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMtKKLGERDPREEILKAFRLFDDDKTGKISLKNL 112
|
90
....*....|....*..
gi 17507545 887 AELVKSLnqtaGVHITE 903
Cdd:PTZ00183 113 KRVAKEL----GETITD 125
|
|
| PLN02964 |
PLN02964 |
phosphatidylserine decarboxylase |
829-890 |
6.42e-03 |
|
phosphatidylserine decarboxylase
Pssm-ID: 215520 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 6.42e-03
10 20 30 40 50 60
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gi 17507545 829 FVKRMFAMTaKHNED-SLSFNEFLTVLREFVNAPQKQKLQTLFKMCDLEGKNKVLRKDLAELV 890
Cdd:PLN02964 180 FARRILAIV-DYDEDgQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALL 241
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| EFh_PI-PLC |
cd15898 |
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
799-937 |
9.40e-03 |
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EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.
Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 38.03 E-value: 9.40e-03
10 20 30 40 50 60 70 80
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gi 17507545 799 SFDSSNDDILN-ETISReeLASAMGMKANNEFVKRMFAMTAKHNEDSLSFNEFLTVLREFVNAPQkqkLQTLFKMCDLEG 877
Cdd:cd15898 8 KADKDGDGKLSlKEIKK--LLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPE---LEPIFKKYAGTN 82
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90 100 110 120 130 140
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gi 17507545 878 KNKVlrkDLAELVKSLNQTAGVHITESVQLRLFNdvlhKSGVSDDAEYLTCNNF-DALFSE 937
Cdd:cd15898 83 RDYM---TLEEFIRFLREEQGENVSEEECEELIE----KYEPERENRQLSFEGFtNFLLSP 136
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